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  Evidence for a Role of VIPP1 in the Structural Organization of the Photosynthetic Apparatus in Chlamydomonas

Nordhues, A., Schöttler, M. A., Unger, A. K., Geimer, S., Schoenfelder, S., Schmollinger, S., et al. (2012). Evidence for a Role of VIPP1 in the Structural Organization of the Photosynthetic Apparatus in Chlamydomonas. The Plant Cell, 24(2), 637-659. doi:10.1105/tpc.111.092692.

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Nordhues, A.1, Author              
Schöttler, M. A.2, Author              
Unger, A. K.3, Author
Geimer, S.3, Author
Schoenfelder, S.1, Author              
Schmollinger, S.1, Author              
Ruetgers, M.1, Author              
Finazzi, G.3, Author
Soppa, B.3, Author
Sommer, F.1, Author              
Muehlhaus, T.1, Author              
Roach, T.3, Author
Krieger-Liszkay, A.3, Author
Lokstein , H.3, Author
Crespo, J. L.3, Author
Schroda, M.1, Author              
Affiliations:
1Plant Molecular Chaperone Networks and Stress, Cooperative Research Groups, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753312              
2Photosynthesis Research, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753323              
3External Organizations, ou_persistent22              

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 Abstract: The vesicle-inducing protein in plastids (VIPP1) was suggested to play a role in thylakoid membrane formation via membrane vesicles. As this functional assignment is under debate, we investigated the function of VIPP1 in Chlamydomonas reinhardtii. Using immunofluorescence, we localized VIPP1 to distinct spots within the chloroplast. In VIPP1-RNA interference/artificial microRNA cells, we consistently observed aberrant, prolamellar body-like structures at the origin of multiple thylakoid membrane layers, which appear to coincide with the immunofluorescent VIPP1 spots and suggest a defect in thylakoid membrane biogenesis. Accordingly, using quantitative shotgun proteomics, we found that unstressed vipp1 mutant cells accumulate 14 to 20% less photosystems, cytochrome b(6)f complex, and ATP synthase but 30% more light-harvesting complex II than control cells, while complex assembly, thylakoid membrane ultrastructure, and bulk lipid composition appeared unaltered. Photosystems in vipp1 mutants are sensitive to high light, which coincides with a lowered midpoint potential of the Q(A)/Q(A)(-) redox couple and increased thermosensitivity of photosystem II (PSII), suggesting structural defects in PSII. Moreover, swollen thylakoids, despite reduced membrane energization, in vipp1 mutants grown on ammonium suggest defects in the supermolecular organization of thylakoid membrane complexes. Overall, our data suggest a role of VIPP1 in the biogenesis/assembly of thylakoid membrane core complexes, most likely by supplying structural lipids.

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Language(s): eng - English
 Dates: 2012-02-072012
 Publication Status: Published in print
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Title: The Plant Cell
  Abbreviation : Plant C
Source Genre: Journal
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Publ. Info: Rockville : American Society of Plant Physiologists
Pages: - Volume / Issue: 24 (2) Sequence Number: - Start / End Page: 637 - 659 Identifier: Other: 1532-298X
CoNE: https://pure.mpg.de/cone/journals/resource/1532-298X